Expression analysis indicated that the gene is reduced by several environmental stresses including high salt, fungus, and abscisic acid, suggesting its possible involvement in multiple stress response pathways. | Turkish Journal of Biology Turk J Biol (2013) 37: 11-17 © TÜBİTAK doi: Research Article Identification and molecular characterization of a receptor-like protein kinase gene from Corchorus capsularis 1, 1, 1 1 Kh. Ambareen REZA **, Sazia SHARMIN **, Mahdi Muhammad MOOSA , Niaz MAHMOOD , 2 1 1, Ajit GHOSH , Rifat Ara BEGUM , Haseena KHAN * 1 Molecular Biology Laboratory, Department of Biochemistry and Molecular Biology, University of Dhaka, Bangladesh 2 International Centre for Genetic Engineering and Biotechnology, New Delhi, India Received: Accepted: Published Online: Printed: Abstract: A leucine-rich repeat-containing protein kinase (LRR-PK) gene has been identified in Corchorus capsularis. This gene, named CcLRR-RLK1, is 3032 bp long and encodes a protein composed of 958 amino acid residues. The deduced peptide contains 3 distinctive domains: a transmembrane domain, 5 leucine-rich repeat-containing motifs, and a serine/threonine protein kinase domain. Expression analysis indicated that the gene is reduced by several environmental stresses including high salt, fungus, and abscisic acid, suggesting its possible involvement in multiple stress response pathways. Key words: Corchorus capsularis, jute, leucine-rich repeat-containing protein kinase, expression analysis 1. Introduction In order to survive in ever-changing environmental conditions, plants have developed several mechanisms to perceive external signals and act accordingly. One such mechanism involves the receptor-like kinases (RLKs), which are involved in the perception and transmission of external stimuli through signaling cascades to elicit appropriate cellular responses (1). The largest group of RLKs includes proteins with leucine-rich repeats (LRRs) that are mainly involved in various protein– protein interactions (2). Most of the LRR-RLKs have an extracellular domain composed of tandem .
